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Volumn 9, Issue 5, 2012, Pages 1425-1434

Differential effects of procaspase-3 activating compounds in the induction of cancer cell death

Author keywords

apoptosis; blood brain barrier; bolus dose; calcium release; constant rate infusion; ER stress; punctate mitochondria; small molecule; transcript profiling; zinc chelation

Indexed keywords

CALCIUM ION; DUAL SPECIFICITY PHOSPHATASE 2; PROCASPASE 3; S PAC 1 PROTEIN; UNCLASSIFIED DRUG;

EID: 84860785721     PISSN: 15438384     EISSN: 15438392     Source Type: Journal    
DOI: 10.1021/mp200673n     Document Type: Article
Times cited : (34)

References (62)
  • 1
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan, D.; Weinberg, R. A. The hallmarks of cancer Cell 2000, 100, 57-70
    • (2000) Cell , vol.100 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 2
    • 79952284127 scopus 로고    scopus 로고
    • Hallmarks of cancer: The next generation
    • Hanahan, D.; Weinberg, R. A. Hallmarks of cancer: the next generation Cell 2011, 144, 646-674
    • (2011) Cell , vol.144 , pp. 646-674
    • Hanahan, D.1    Weinberg, R.A.2
  • 9
    • 1842636513 scopus 로고    scopus 로고
    • Increased expression of Apaf-1 and procaspase-3 and the functionality of intrinsic apoptosis apparatus in non-small cell lung carcinoma
    • Krepela, E.; Prochazka, J.; Liul, X.; Fiala, P.; Kinkor, Z. Increased expression of Apaf-1 and procaspase-3 and the functionality of intrinsic apoptosis apparatus in non-small cell lung carcinoma Biol. Chem. 2004, 385, 153-168
    • (2004) Biol. Chem. , vol.385 , pp. 153-168
    • Krepela, E.1    Prochazka, J.2    Liul, X.3    Fiala, P.4    Kinkor, Z.5
  • 10
    • 77955977688 scopus 로고    scopus 로고
    • Upregulation of caspase-3 expression in esophageal cancer correlates with favorable prognosis: An immunohistochemical study from a high incidence area in northern China
    • Jiang, H.; Gong, M.; Cui, Y.; Ma, K.; Chang, D.; Wang, T. Y. Upregulation of caspase-3 expression in esophageal cancer correlates with favorable prognosis: an immunohistochemical study from a high incidence area in northern China Dis. Esophagus 2010, 23, 487-492
    • (2010) Dis. Esophagus , vol.23 , pp. 487-492
    • Jiang, H.1    Gong, M.2    Cui, Y.3    Ma, K.4    Chang, D.5    Wang, T.Y.6
  • 12
    • 0032588953 scopus 로고    scopus 로고
    • Characterization of the interleukin-1beta-converting enzyme/ced-3-family protease, caspase-3/CPP32, in Hodgkin's disease: Lack of caspase-3 expression in nodular lymphocyte predominance Hodgkin's disease
    • Izban, K. F.; Wrone-Smith, T.; Hsi, E. D.; Schnitzer, B.; Quevedo, M. E.; Alkan, S. Characterization of the interleukin-1beta-converting enzyme/ced-3-family protease, caspase-3/CPP32, in Hodgkin's disease: lack of caspase-3 expression in nodular lymphocyte predominance Hodgkin's disease Am. J. Pathol. 1999, 154, 1439-1447
    • (1999) Am. J. Pathol. , vol.154 , pp. 1439-1447
    • Izban, K.F.1    Wrone-Smith, T.2    Hsi, E.D.3    Schnitzer, B.4    Quevedo, M.E.5    Alkan, S.6
  • 13
    • 80054017688 scopus 로고    scopus 로고
    • Immunohistochemical expression of procaspase-3 and its clinical significance in childhood non-Hodgkin lymphomas
    • Wrobel, G.; Maldyk, J.; Kazanowska, B.; Rapala, M.; Maciejka-Kapuscinska, L.; Chaber, R. Immunohistochemical expression of procaspase-3 and its clinical significance in childhood non-Hodgkin lymphomas Pediatr. Dev. Pathol. 2011, 14, 173-179
    • (2011) Pediatr. Dev. Pathol. , vol.14 , pp. 173-179
    • Wrobel, G.1    Maldyk, J.2    Kazanowska, B.3    Rapala, M.4    MacIejka-Kapuscinska, L.5    Chaber, R.6
  • 18
    • 70349433777 scopus 로고    scopus 로고
    • Procaspase-3 Activation as an Anti-Cancer Strategy: Structure-Activity Relationship of PAC-1, and its Cellular Co-Localization with Procaspase-3
    • Peterson, Q. P.; Hsu, D. C.; Goode, D. R.; Novotny, C. J.; Totten, R. K.; Hergenrother, P. J. Procaspase-3 Activation as an Anti-Cancer Strategy: Structure-Activity Relationship of PAC-1, and its Cellular Co-Localization with Procaspase-3 J. Med. Chem. 2009, 52, 5721-5731
    • (2009) J. Med. Chem. , vol.52 , pp. 5721-5731
    • Peterson, Q.P.1    Hsu, D.C.2    Goode, D.R.3    Novotny, C.J.4    Totten, R.K.5    Hergenrother, P.J.6
  • 19
    • 84855580303 scopus 로고    scopus 로고
    • Parallel synthesis and biological evaluation of 837 analogues of procaspase-activating compound 1 (PAC-1)
    • Hsu, D. C.; Roth, H. S.; West, D. C.; Botham, R. C.; Novotny, C. J.; Schmid, S. C.; Hergenrother, P. J. Parallel synthesis and biological evaluation of 837 analogues of procaspase-activating compound 1 (PAC-1) ACS Comb. Sci. 2012, 14, 44-50
    • (2012) ACS Comb. Sci. , vol.14 , pp. 44-50
    • Hsu, D.C.1    Roth, H.S.2    West, D.C.3    Botham, R.C.4    Novotny, C.J.5    Schmid, S.C.6    Hergenrother, P.J.7
  • 20
    • 70449372265 scopus 로고    scopus 로고
    • Small-molecule activators of a proenzyme
    • Wolan, D. W.; Zorn, J. A.; Gray, D. C.; Wells, J. A. Small-molecule activators of a proenzyme Science 2009, 326, 853-858
    • (2009) Science , vol.326 , pp. 853-858
    • Wolan, D.W.1    Zorn, J.A.2    Gray, D.C.3    Wells, J.A.4
  • 21
    • 83055197029 scopus 로고    scopus 로고
    • Self-assembling small molecules form nanofibrils that bind procaspase-3 to promote activation
    • Zorn, J. A.; Wille, H.; Wolan, D. W.; Wells, J. A. Self-assembling small molecules form nanofibrils that bind procaspase-3 to promote activation J. Am. Chem. Soc. 2011, 133, 19630-19633
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 19630-19633
    • Zorn, J.A.1    Wille, H.2    Wolan, D.W.3    Wells, J.A.4
  • 22
    • 79956297378 scopus 로고    scopus 로고
    • Measuring steady-state and dynamic endoplasmic reticulum and Golgi Zn2+ with genetically encoded sensors
    • Qin, Y.; Dittmer, P. J.; Park, J. G.; Jansen, K. B.; Palmer, A. E. Measuring steady-state and dynamic endoplasmic reticulum and Golgi Zn2+ with genetically encoded sensors Proc. Natl. Acad. Sci. U.S.A. 2011, 108, 7351-7356
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 7351-7356
    • Qin, Y.1    Dittmer, P.J.2    Park, J.G.3    Jansen, K.B.4    Palmer, A.E.5
  • 25
    • 77951081423 scopus 로고    scopus 로고
    • Chemistry and biology of deoxynyboquinone, a potent inducer of cancer cell death
    • Bair, J. S.; Palchaudhuri, R.; Hergenrother, P. J. Chemistry and biology of deoxynyboquinone, a potent inducer of cancer cell death J. Am. Chem. Soc. 2010, 132, 5469-5478
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 5469-5478
    • Bair, J.S.1    Palchaudhuri, R.2    Hergenrother, P.J.3
  • 26
    • 67650257938 scopus 로고    scopus 로고
    • Genetically encoded sensors to elucidate spatial distribution of cellular zinc
    • Dittmer, P. J.; Miranda, J. G.; Gorski, J. A.; Palmer, A. E. Genetically encoded sensors to elucidate spatial distribution of cellular zinc J. Biol. Chem. 2009, 284, 16289-16297
    • (2009) J. Biol. Chem. , vol.284 , pp. 16289-16297
    • Dittmer, P.J.1    Miranda, J.G.2    Gorski, J.A.3    Palmer, A.E.4
  • 28
    • 79251508332 scopus 로고    scopus 로고
    • Transcript profiling and RNA interference as tools to identify small molecule mechanisms and therapeutic potential
    • Palchaudhuri, R.; Hergenrother, P. J. Transcript profiling and RNA interference as tools to identify small molecule mechanisms and therapeutic potential ACS Chem. Biol. 2011, 6, 21-33
    • (2011) ACS Chem. Biol. , vol.6 , pp. 21-33
    • Palchaudhuri, R.1    Hergenrother, P.J.2
  • 29
    • 71549129296 scopus 로고    scopus 로고
    • Improving gene expression similarity measurement using pathway-based analytic dimension
    • Keum, C.; Woo, J. H.; Oh, W. S.; Park, S. N.; No, K. T. Improving gene expression similarity measurement using pathway-based analytic dimension BMC Genomics 2009, 10 (Suppl. 3) S15
    • (2009) BMC Genomics , vol.10 , Issue.SUPPL. 3 , pp. 15
    • Keum, C.1    Woo, J.H.2    Oh, W.S.3    Park, S.N.4    No, K.T.5
  • 30
    • 77956828961 scopus 로고    scopus 로고
    • Distinct gene expression profiles characterize cellular responses to palmitate and oleate
    • Das, S. K.; Mondal, A. K.; Elbein, S. C. Distinct gene expression profiles characterize cellular responses to palmitate and oleate J. Lipid Res. 2010, 51, 2121-2131
    • (2010) J. Lipid Res. , vol.51 , pp. 2121-2131
    • Das, S.K.1    Mondal, A.K.2    Elbein, S.C.3
  • 31
    • 1842843855 scopus 로고    scopus 로고
    • Roles of CHOP/GADD153 in endoplasmic reticulum stress
    • Oyadomari, S.; Mori, M. Roles of CHOP/GADD153 in endoplasmic reticulum stress Cell Death Differ. 2004, 11, 381-389
    • (2004) Cell Death Differ. , vol.11 , pp. 381-389
    • Oyadomari, S.1    Mori, M.2
  • 32
    • 0034693217 scopus 로고    scopus 로고
    • Herp, a new ubiquitin-like membrane protein induced by endoplasmic reticulum stress
    • Kokame, K.; Agarwala, K. L.; Kato, H.; Miyata, T. Herp, a new ubiquitin-like membrane protein induced by endoplasmic reticulum stress J. Biol. Chem. 2000, 275, 32846-32853
    • (2000) J. Biol. Chem. , vol.275 , pp. 32846-32853
    • Kokame, K.1    Agarwala, K.L.2    Kato, H.3    Miyata, T.4
  • 34
    • 0031960313 scopus 로고    scopus 로고
    • A tool coming of age: Thapsigargin as an inhibitor of sarco-endoplasmic reticulum Ca(2+)-ATPases
    • Treiman, M.; Caspersen, C.; Christensen, S. B. A tool coming of age: thapsigargin as an inhibitor of sarco-endoplasmic reticulum Ca(2+)-ATPases Trends Pharmacol. Sci. 1998, 19, 131-135
    • (1998) Trends Pharmacol. Sci. , vol.19 , pp. 131-135
    • Treiman, M.1    Caspersen, C.2    Christensen, S.B.3
  • 35
    • 33748789479 scopus 로고    scopus 로고
    • Mediators of endoplasmic reticulum stress-induced apoptosis
    • Szegezdi, E.; Logue, S. E.; Gorman, A. M.; Samali, A. Mediators of endoplasmic reticulum stress-induced apoptosis EMBO Rep. 2006, 7, 880-885
    • (2006) EMBO Rep. , vol.7 , pp. 880-885
    • Szegezdi, E.1    Logue, S.E.2    Gorman, A.M.3    Samali, A.4
  • 36
    • 70349905357 scopus 로고    scopus 로고
    • Role of ERO1-alpha-mediated stimulation of inositol 1,4,5-triphosphate receptor activity in endoplasmic reticulum stress-induced apoptosis
    • Li, G.; Mongillo, M.; Chin, K. T.; Harding, H.; Ron, D.; Marks, A. R.; Tabas, I. Role of ERO1-alpha-mediated stimulation of inositol 1,4,5-triphosphate receptor activity in endoplasmic reticulum stress-induced apoptosis J. Cell Biol. 2009, 186, 783-792
    • (2009) J. Cell Biol. , vol.186 , pp. 783-792
    • Li, G.1    Mongillo, M.2    Chin, K.T.3    Harding, H.4    Ron, D.5    Marks, A.R.6    Tabas, I.7
  • 37
    • 0037204545 scopus 로고    scopus 로고
    • Computational approaches to the prediction of the blood-brain distribution
    • Norinder, U.; Haeberlein, M. Computational approaches to the prediction of the blood-brain distribution Adv. Drug Delivery Rev. 2002, 54, 291-313
    • (2002) Adv. Drug Delivery Rev. , vol.54 , pp. 291-313
    • Norinder, U.1    Haeberlein, M.2
  • 38
    • 0141958109 scopus 로고    scopus 로고
    • In silico prediction of blood-brain barrier permeation
    • Clark, D. E. In silico prediction of blood-brain barrier permeation Drug Discovery Today 2003, 8, 927-933
    • (2003) Drug Discovery Today , vol.8 , pp. 927-933
    • Clark, D.E.1
  • 39
    • 1242269804 scopus 로고    scopus 로고
    • Apoptosis induced by endoplasmic reticulum stress depends on activation of caspase-3 via caspase-12
    • Hitomi, J.; Katayama, T.; Taniguchi, M.; Honda, A.; Imaizumi, K.; Tohyama, M. Apoptosis induced by endoplasmic reticulum stress depends on activation of caspase-3 via caspase-12 Neurosci. Lett. 2004, 357, 127-130
    • (2004) Neurosci. Lett. , vol.357 , pp. 127-130
    • Hitomi, J.1    Katayama, T.2    Taniguchi, M.3    Honda, A.4    Imaizumi, K.5    Tohyama, M.6
  • 40
    • 24344433558 scopus 로고    scopus 로고
    • Induction of endoplasmic reticulum stress and apoptosis by a marine prostanoid in human hepatocellular carcinoma
    • Chiang, P. C.; Chien, C. L.; Pan, S. L.; Chen, W. P.; Teng, C. M.; Shen, Y. C.; Guh, J. H. Induction of endoplasmic reticulum stress and apoptosis by a marine prostanoid in human hepatocellular carcinoma J. Hepatol. 2005, 43, 679-686
    • (2005) J. Hepatol. , vol.43 , pp. 679-686
    • Chiang, P.C.1    Chien, C.L.2    Pan, S.L.3    Chen, W.P.4    Teng, C.M.5    Shen, Y.C.6    Guh, J.H.7
  • 41
    • 26844570219 scopus 로고    scopus 로고
    • Lysosomes and endoplasmic reticulum: Targets for improved, selective anticancer therapy
    • Linder, S.; Shoshan, M. C. Lysosomes and endoplasmic reticulum: targets for improved, selective anticancer therapy Drug Resist. Updates 2005, 8, 199-204
    • (2005) Drug Resist. Updates , vol.8 , pp. 199-204
    • Linder, S.1    Shoshan, M.C.2
  • 43
    • 34347386472 scopus 로고    scopus 로고
    • Thapsigargin induces biphasic fragmentation of mitochondria through calcium-mediated mitochondrial fission and apoptosis
    • Hom, J. R.; Gewandter, J. S.; Michael, L.; Sheu, S. S.; Yoon, Y. Thapsigargin induces biphasic fragmentation of mitochondria through calcium-mediated mitochondrial fission and apoptosis J. Cell. Physiol. 2007, 212, 498-508
    • (2007) J. Cell. Physiol. , vol.212 , pp. 498-508
    • Hom, J.R.1    Gewandter, J.S.2    Michael, L.3    Sheu, S.S.4    Yoon, Y.5
  • 47
    • 79954426157 scopus 로고    scopus 로고
    • Signaling cell death from the endoplasmic reticulum stress response
    • Shore, G. C.; Papa, F. R.; Oakes, S. A. Signaling cell death from the endoplasmic reticulum stress response Curr. Opin. Cell Biol. 2011, 23, 143-149
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 143-149
    • Shore, G.C.1    Papa, F.R.2    Oakes, S.A.3
  • 49
    • 80053418778 scopus 로고    scopus 로고
    • Essential requirement of cytochrome c release for caspase activation by procaspase-activating compound defined by cellular models
    • 210.1038/cddis.2011.1090
    • Seervi, M.; Joseph, J.; Sobhan, P. K.; Bhavya, B. C.; Santhoshkumar, T. R. Essential requirement of cytochrome c release for caspase activation by procaspase-activating compound defined by cellular models Cell Death Dis. 2011, 2, e207 210.1038/cddis.2011.1090
    • (2011) Cell Death Dis. , vol.2 , pp. 207
    • Seervi, M.1    Joseph, J.2    Sobhan, P.K.3    Bhavya, B.C.4    Santhoshkumar, T.R.5
  • 50
    • 0030724177 scopus 로고    scopus 로고
    • Tunicamycin increases intracellular calcium levels in bovine aortic endothelial cells
    • Buckley, B. J.; Whorton, A. R. Tunicamycin increases intracellular calcium levels in bovine aortic endothelial cells Am. J. Physiol. 1997, 273, C1298-1305
    • (1997) Am. J. Physiol. , vol.273 , pp. 1298-1305
    • Buckley, B.J.1    Whorton, A.R.2
  • 51
    • 0037417334 scopus 로고    scopus 로고
    • Caspase cleavage product of BAP31 induces mitochondrial fission through endoplasmic reticulum calcium signals, enhancing cytochrome c release to the cytosol
    • Breckenridge, D. G.; Stojanovic, M.; Marcellus, R. C.; Shore, G. C. Caspase cleavage product of BAP31 induces mitochondrial fission through endoplasmic reticulum calcium signals, enhancing cytochrome c release to the cytosol J. Cell Biol. 2003, 160, 1115-1127
    • (2003) J. Cell Biol. , vol.160 , pp. 1115-1127
    • Breckenridge, D.G.1    Stojanovic, M.2    Marcellus, R.C.3    Shore, G.C.4
  • 52
    • 3242675057 scopus 로고    scopus 로고
    • Association of active caspase 8 with the mitochondrial membrane during apoptosis: Potential roles in cleaving BAP31 and caspase 3 and mediating mitochondrion-endoplasmic reticulum cross talk in etoposide-induced cell death
    • Chandra, D.; Choy, G.; Deng, X.; Bhatia, B.; Daniel, P.; Tang, D. G. Association of active caspase 8 with the mitochondrial membrane during apoptosis: potential roles in cleaving BAP31 and caspase 3 and mediating mitochondrion-endoplasmic reticulum cross talk in etoposide-induced cell death Mol. Cell. Biol. 2004, 24, 6592-6607
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 6592-6607
    • Chandra, D.1    Choy, G.2    Deng, X.3    Bhatia, B.4    Daniel, P.5    Tang, D.G.6
  • 53
    • 0035957929 scopus 로고    scopus 로고
    • Activation of caspase-12, an endoplastic reticulum (ER) resident caspase, through tumor necrosis factor receptor-associated factor 2-dependent mechanism in response to the ER stress
    • Yoneda, T.; Imaizumi, K.; Oono, K.; Yui, D.; Gomi, F.; Katayama, T.; Tohyama, M. Activation of caspase-12, an endoplastic reticulum (ER) resident caspase, through tumor necrosis factor receptor-associated factor 2-dependent mechanism in response to the ER stress J. Biol. Chem. 2001, 276, 13935-13940
    • (2001) J. Biol. Chem. , vol.276 , pp. 13935-13940
    • Yoneda, T.1    Imaizumi, K.2    Oono, K.3    Yui, D.4    Gomi, F.5    Katayama, T.6    Tohyama, M.7
  • 55
    • 36348943088 scopus 로고    scopus 로고
    • Integrated endoplasmic reticulum stress responses in cancer
    • Moenner, M.; Pluquet, O.; Bouchecareilh, M. Chevet, E., Integrated endoplasmic reticulum stress responses in cancer Cancer Res. 2007, 67, 10631-10634
    • (2007) Cancer Res. , vol.67 , pp. 10631-10634
    • Moenner, M.1    Pluquet, O.2    Bouchecareilh, M.3    Chevet, E.4
  • 57
    • 79952982043 scopus 로고    scopus 로고
    • Targeting ER stress induced apoptosis and inflammation in cancer
    • 10.1016/j.canlet.2010.1007.1016
    • Verfaillie, T.; Garg, A. D.; Agostinis, P. Targeting ER stress induced apoptosis and inflammation in cancer Cancer Lett. 2010, 10.1016/j.canlet.2010. 1007.1016
    • (2010) Cancer Lett.
    • Verfaillie, T.1    Garg, A.D.2    Agostinis, P.3
  • 58
    • 77953024622 scopus 로고    scopus 로고
    • Progress in the unraveling of the endoplasmic reticulum stress/autophagy pathway and cancer: Implications for future therapeutic approaches
    • Schleicher, S. M.; Moretti, L.; Varki, V.; Lu, B. Progress in the unraveling of the endoplasmic reticulum stress/autophagy pathway and cancer: implications for future therapeutic approaches Drug Resist. Updates 2010, 13, 79-86
    • (2010) Drug Resist. Updates , vol.13 , pp. 79-86
    • Schleicher, S.M.1    Moretti, L.2    Varki, V.3    Lu, B.4
  • 60
    • 0030450126 scopus 로고    scopus 로고
    • Short exposures to tunicamycin induce apoptosis in SV40-transformed but not in normal human fibroblasts
    • Carlberg, M.; Dricu, A.; Blegen, H.; Kass, G. E.; Orrenius, S.; Larsson, O. Short exposures to tunicamycin induce apoptosis in SV40-transformed but not in normal human fibroblasts Carcinogenesis 1996, 17, 2589-2596
    • (1996) Carcinogenesis , vol.17 , pp. 2589-2596
    • Carlberg, M.1    Dricu, A.2    Blegen, H.3    Kass, G.E.4    Orrenius, S.5    Larsson, O.6
  • 61
    • 56849117387 scopus 로고    scopus 로고
    • Transient potent BCR-ABL inhibition is sufficient to commit chronic myeloid leukemia cells irreversibly to apoptosis
    • Shah, N. P.; Kasap, C.; Weier, C.; Balbas, M.; Nicoll, J. M.; Bleickardt, E.; Nicaise, C.; Sawyers, C. L. Transient potent BCR-ABL inhibition is sufficient to commit chronic myeloid leukemia cells irreversibly to apoptosis Cancer Cell 2008, 14, 485-493
    • (2008) Cancer Cell , vol.14 , pp. 485-493
    • Shah, N.P.1    Kasap, C.2    Weier, C.3    Balbas, M.4    Nicoll, J.M.5    Bleickardt, E.6    Nicaise, C.7    Sawyers, C.L.8
  • 62
    • 77956823937 scopus 로고    scopus 로고
    • Dasatinib in imatinib-resistant or imatinib-intolerant chronic myeloid leukemia in blast phase after 2 years of follow-up in a phase 3 study: Efficacy and tolerability of 140 mg once daily and 70 mg twice daily
    • Saglio, G.; Hochhaus, A.; Goh, Y. T.; Masszi, T.; Pasquini, R.; Maloisel, F.; Erben, P.; Cortes, J.; Paquette, R.; Bradley-Garelik, M. B.; Zhu, C.; Dombret, H. Dasatinib in imatinib-resistant or imatinib-intolerant chronic myeloid leukemia in blast phase after 2 years of follow-up in a phase 3 study: efficacy and tolerability of 140 mg once daily and 70 mg twice daily Cancer 2010, 116, 3852-3861
    • (2010) Cancer , vol.116 , pp. 3852-3861
    • Saglio, G.1    Hochhaus, A.2    Goh, Y.T.3    Masszi, T.4    Pasquini, R.5    Maloisel, F.6    Erben, P.7    Cortes, J.8    Paquette, R.9    Bradley-Garelik, M.B.10    Zhu, C.11    Dombret, H.12


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